ID A0A2G8RTV2_9APHY Unreviewed; 1547 AA.
AC A0A2G8RTV2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=GSI_12816 {ECO:0000313|EMBL:PIL24929.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL24929.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL24929.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL24929.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIL24929.1}.
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DR EMBL; AYKW01000056; PIL24929.1; -; Genomic_DNA.
DR STRING; 1077348.A0A2G8RTV2; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000230002; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..982
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1061..1086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1255..1276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1351..1370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1443..1465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1477..1499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..61
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 8..55
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 232..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..662
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1547 AA; 173942 MW; 78F10AC4E3FD5665 CRC64;
MQEEQDTCRI CSAPAEPEQP LFYPCKCSGT IRYIHQDCLT EWLAHSKKKT CDVCKHPYSF
TKVYSKDMPE RLPILLVMRQ FSRQIVSAIL FGLRAALVAT VWLAALPWST IWTWRMYFAL
GNSAAWWISA VKRDASDVDF YPATVPNSST VNATSTNTTD AQPSSSPSLF SHPLYRTISS
DIFSGQIIAS IIVLTFVAIF LLREWITQNA RPGVFEDGDA GVEPVADALP PLPELPQPQP
PVHLAPPALP RPPSPPPIVA ELVHERAIPI RDDRYVPRDD LPFQARTKKP RTRGDVYASE
DSQEAGPSHV GKGKRRAHTT AREERRTLRR RRIGRRTRMF DGDESHDESM GLHDDKDFRR
LRYVAHRAGD FDDELRRRNG RSSMSEPEKW PPERNHKHPR DPNRLPAFSE FTFTYPSPST
TNWDGRSPSP PGFASDPPAH NPFARSLSRL DIDSEDDEDE RERTPTRPST PILGASPSGS
YDLIDAEDFE AIAGSAQAST STTGLRRPPL PTMTLPPSPI PSISVEVVRG ATPLESPSLA
TYRAPEELDA DAAADRDYFV HDDDDDLQQD QLLDHEQTEE EHAYYFRDPS ENDTDFDTDE
EEEARARVQQ DVEAQRVRAQ EMAEMADEEL DMDDEGEIDM DDLQWTDDDP LHEDDDDEEG
EGGQGVVQIR EELPGPFAGG QPPEPPLPQD DFDAEVNIED DMDGALEAIG LRGPLVGVLQ
NAVLMTFILD TTIGLGIWLP FTIGKSTALL TLNPRRAVQL VHLPLRLIRL VTDPIVDSVL
LLISKLLLPS LAHFGQAALC SGLRIIASAL GQDRADKLAE LSTDAYDNVL AVASQIMNRT
TPLTYSPSDV SVTESLSSTL YRALEEDTTV MRVVEPYFAP LGKNVREWFG EGKTSWVRFA
TGDTPNDRAF AVVLGYTVVG LLLAIYLNVL TVGSMRSASR AVRNAVRQQL LVVKVAAFIV
VELVVFPLGC GVMLDVCTVW LFPQGSFRSR AAFLMYAPLT AVFYHWVLGT MFMYQFAVLL
SGCRGIMRPG AMWFIKDPQD QNFHPIRDIL ERPTLTQIRK LVLSAMMYGF VVASGVATVS
GILRIFSRTI MPFRWKIREP LSEVPIDLIL LQLVLPYTME SFRPRKALRR FGSFIWRYLA
SRLRLSSYMF GGRFNAEEFT PKHWSWRSLL IQDGIQMDDD EAPHDGGFRR VPNSDNVALV
RNSPATALVL EDGTPIDEAA RQLIDAQNAE AQKQKRPIKD DYTVVYIPPN FRYRVITFLV
CLWTIGSVML ASVLAAPILM GRGFFRLFIS HDVHDGYSFI VGFYLIWACW LISASLDRMD
KRRQRRWSGT DPRAEWALFV VKRALLWIAQ ALYMTVTLGI IVPTLVGLVF ELYIVQPIRH
TANPLMEPRI RLVDMWALGL LYSKIIIRTL RMHPPTHGLM HGIDRLVRNG WTHLDPMRAT
KDVILPLIAG LTGMIVLPAA ALWGLQRAVT LPMDGDFLFL HVYPGIFTAA GLVHGAFALS
KVLGSWSQTI RDKEFLVEMR LRNLEPDQDK SVEQQEDAKE VVTEVEE
//
